BETB_PSEA8
ID BETB_PSEA8 Reviewed; 490 AA.
AC B7V5R4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Betaine aldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00804};
DE Short=BADH {ECO:0000255|HAMAP-Rule:MF_00804};
DE EC=1.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00804};
GN Name=betB {ECO:0000255|HAMAP-Rule:MF_00804}; OrderedLocusNames=PLES_57681;
OS Pseudomonas aeruginosa (strain LESB58).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=557722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LESB58;
RX PubMed=19047519; DOI=10.1101/gr.086082.108;
RA Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT "Newly introduced genomic prophage islands are critical determinants of in
RT vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT aeruginosa.";
RL Genome Res. 19:12-23(2009).
CC -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine
CC betaine. Catalyzes the irreversible oxidation of betaine aldehyde to
CC the corresponding acid. {ECO:0000255|HAMAP-Rule:MF_00804}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.8; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00804};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00804};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00804};
CC Note=Binds 2 potassium ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00804};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine from betaine aldehyde: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00804}.
CC -!- SUBUNIT: Dimer of dimers. {ECO:0000255|HAMAP-Rule:MF_00804}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_00804}.
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DR EMBL; FM209186; CAW30522.1; -; Genomic_DNA.
DR RefSeq; WP_003114436.1; NC_011770.1.
DR AlphaFoldDB; B7V5R4; -.
DR SMR; B7V5R4; -.
DR KEGG; pag:PLES_57681; -.
DR HOGENOM; CLU_005391_0_2_6; -.
DR OMA; GMKYVTM; -.
DR UniPathway; UPA00529; UER00386.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR HAMAP; MF_00804; BADH; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR011264; BADH.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01804; BADH; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Metal-binding; NAD; NADP; Oxidation; Oxidoreductase; Potassium.
FT CHAIN 1..490
FT /note="Betaine aldehyde dehydrogenase"
FT /id="PRO_1000133955"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT ACT_SITE 252
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT ACT_SITE 286
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT ACT_SITE 464
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 26
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 27
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 93
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 150..152
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 176..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 180
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 230..233
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 246
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 254
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 286
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /note="covalent"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 387
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 457
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT BINDING 460
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT SITE 248
FT /note="Seems to be a necessary countercharge to the
FT potassium cations"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT MOD_RES 286
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
SQ SEQUENCE 490 AA; 53332 MW; F48249A085E3A970 CRC64;
MARFEEQKLY IGGRYVEASS GATFETINPA NGEVLAKVQR ASREDVERAV QSAVEGQKVW
AAMTAMQRSR ILRRAVDILR ERNDELAALE TLDTGKPLAE TRSVDIVTGA DVLEYYAGLV
PAIEGEQIPL RETSFVYTRR EPLGVVAGIG AWNYPVQIAL WKSAPALAAG NAMIFKPSEV
TPLTALKLAE IYTEAGVPDG VFNVLTGSGR EVGQWLTEHP LIEKISFTGG TSTGKKVMAS
ASSSSLKEVT MELGGKSPLI IFPDADLDRA ADIAVMANFF SSGQVCTNGT RVFIHRSQQA
RFEAKVLERV QRIRLGDPQD ENTNFGPLVS FPHMESVLGY IESGKAQKAR LLCGGERVTD
GAFGKGAYVA PTVFTDCRDD MTIVREEIFG PVMSILVYDD EDEAIRRAND TEYGLAAGVV
TQDLARAHRA IHRLEAGICW INTWGESPAE MPVGGYKQSG VGRENGLTTL AHYTRIKSVQ
VELGDYASVF
